Open AccessBovine serum albumin refolding at acid solution by small angle neutron scattering
Author(s) -
Arum Patriati,
Nadi Suparno,
Edy Giri Rachman Putra
Publication year - 2021
Publication title -
journal of physics. conference series
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.21
H-Index - 85
eISSN - 1742-6596
pISSN - 1742-6588
DOI - 10.1088/1742-6596/1825/1/012051
Subject(s) - sorbitol , bovine serum albumin , small angle neutron scattering , chemistry , scattering , small angle x ray scattering , neutron scattering , small angle scattering , crystallography , serum albumin , ionic strength , chromatography , analytical chemistry (journal) , organic chemistry , optics , biochemistry , physics , aqueous solution
A series of study of the conformational change of bovine serum albumin (BSA) induced by pH and additive has been conducted by small angle scattering (SANS) technique. The unfolding process occur by increasing the solvent acidity of the buffer. The previous work from SANS scattering profile shows that BSA unfolded into a cylinder-like structure at pH 2. In this work, the role of sorbitol in refolding process of BSA in acid solution was studied. Sorbitol, at concentrations from 0 to 3 M, led to the progressive restoration of BSA globular structure. The SANS scattering data show the conformational change from cylinder-like structure of pure BSA at pH 2 undergo to ellipsoid-like structure in the addition of 3M sorbitol. In the absence, 1M and 2M sorbitol, the SANS scattering profile of BSA fitted to flexible cylinder model. Meanwhile in the present of 3M sorbitol, it fitted to triaxial ellipsoid model. These results are confirmed with ab initio low-resolution shape calculation model analysis using GNOM and DAMMIN obtaining the three-dimensional structure model.